5d6w

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m (Protected "5d6w" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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==Crystal structure of double tudor domain of human lysine demethylase KDM4A==
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<StructureSection load='5d6w' size='340' side='right' caption='[[5d6w]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
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The entry 5d6w is ON HOLD
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5d6w]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D6W FirstGlance]. <br>
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Authors: Wang, F., Su, Z., Denu, J.M., Phillips Jr., G.N., Enzyme Discovery for Natural Product Biosynthesis (NatPro)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d6x|5d6x]], [[5d6y|5d6y]]</td></tr>
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Description: Crystal structure of double tudor domain of human lysine demethylase KDM4A
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d6w OCA], [http://pdbe.org/5d6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d6w RCSB], [http://www.ebi.ac.uk/pdbsum/5d6w PDBsum]</span></td></tr>
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[[Category: Unreleased Structures]]
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</table>
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[[Category: G.N]]
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== Function ==
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[[http://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Denu, J M]]
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[[Category: NatPro, Enzyme Discovery for Natural Product Biosynthesis]]
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[[Category: Phillips, G N]]
[[Category: Su, Z]]
[[Category: Su, Z]]
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[[Category: Denu, J.M]]
 
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[[Category: Enzyme Discovery For Natural Product Biosynthesis (Natpro)]]
 
[[Category: Wang, F]]
[[Category: Wang, F]]
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[[Category: Phillips Jr]]
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[[Category: Double tudor domain]]
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[[Category: Enzyme discovery for natural product biosynthesis]]
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[[Category: Natpro]]
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[[Category: Oxidoreductase]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Reader domain]]
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[[Category: Structural genomic]]

Revision as of 04:44, 1 December 2015

Crystal structure of double tudor domain of human lysine demethylase KDM4A

5d6w, resolution 1.99Å

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